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2.5.1.113 |
Description |
[CysO sulfur-carrier protein]-thiocarboxylate-dependent cysteine synthase |
Alternative names |
O-phospho-L-serine:thiocarboxylated [CysO sulfur-carrier protein] 2-amino-2-carboxyethyltransferase;
CysM. |
Catalyzed reaction |
O-phospho-L-serine + [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)SH = [CysO sulfur-carrier protein]-Gly-NH-CH2-C(O)-S-L-cysteine + phosphate |
Cofactor |
Pyridoxal-phosphate. |
Comments |
A pyridoxal-phosphate protein. The enzyme participates in an alternative pathway for L-cysteine biosynthesis that involves a protein-bound thiocarboxylate as the sulfide donor. The enzyme from the bacterium Mycobacterium tuberculosis also has very low activity with O3-acetyl-L-serine (cf. EC 2.5.1.65, O-phosphoserine sulfhydrylase). |
PDB |
3DKI; 3DWG; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.5.1.113
BRENDA (activities) 2.5.1.113
KEGG (pathways) 2.5.1.113
PLPMDB (PLP mutants) 2.5.1.113
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References |
Agren D, Schnell R, Oehlmann W, Singh M, Schneider G.
(2008) Cysteine Synthase (CysM) of Mycobacterium tuberculosis Is an O-Phosphoserine Sulfhydrylase: evidence for an alternative cysteine biosynthesis pathway in mycobacteria. J Biol Chem 283 31567-74. Jurgenson CT1, Burns KE, Begley TP, Ealick SE.
(2008) Crystal structure of a sulfur carrier protein complex found in the cysteine biosynthetic pathway of Mycobacterium tuberculosis. Biochemistry 47 10354-64. O'Leary SE, Jurgenson CT, Begley TP, Ealick SE.
(2008) O-phospho-L-serine and the thiocarboxylated sulfur carrier protein CysO-COSH are substrates for CysM, a cysteine synthase from Mycobacterium tuberculosis. Biochemistry 47 11606-15. Articles on 2.5.1.113 |
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last changed |
2019/06/21 13:02 |
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